Introduction
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Navigate through the different steps using the tabs available at the top of the dashboard.

Phytase Introduction

Why phytase placeholder.

The Process

Placeholder describing theoretical design. 1. Conserving residues involved in activity based on proximity to ligand and evolutionary conservation. 2. Maintain these residues and generate remainder of protein sequence. 3. Structural prediction and overlay with natural phytase. 4. Comparison of key enzymatic characteristics; confidence predictions, pH activity, solubility.

Identify residues located near ligand, and conserved across evolutionary phytases.

The 3D visualization of E. coli phytase (PDB: 1DKP) is shown bound to its natural substrate, inositol hexakisphosphate (IHP), highlighting amino acid residues nearby the ligand.

Distance of Amino Acid Residue from Nearest Ligand Molecule
3D Protein Structure (1DKP)
Visualization Features

This dashboard presents a visual representation of the Phytase (1DKP) crystal structure bound to it’s phytate ligand (IHP).

The scatter plot represents the alpha-carbon and ligand atom locations in 3-dimensional space.

  • Gray markers: All protein residues
  • Green markers: Residues within 7Å of the ligand
  • Purple markers: IHP ligand atoms
Protein Summary Metrics
Property Value
Total Residues 310
Proximal Residues (≤7Å) 39
Ligand Atoms 36
Proximity Threshold 7.0 Å

Placeholder for comparing the predicted protein to the original 1DKP structure.